|
Name |
Accession |
Description |
Interval |
E-value |
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
9-399 |
0e+00 |
|
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB.
Pssm-ID: 349898 [Multi-domain] Cd Length: 391 Bit Score: 757.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 9 EHPSVTLFRQYLRICTVQPNPDYGSAVTFLEERARQLGLSCQKIEVAPGYVITVLTWPGTNPLLHSILLNSHTDVVPVFK 88
Cdd:cd05646 1 EDPAVTRFREYLRINTVHPNPDYDACVEFLKRQADELGLPVRVIEVVPGKPVVVLTWEGSNPELPSILLNSHTDVVPVFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 89 EHWHHDPFEAFKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFVKRPEFQALR 168
Cdd:cd05646 81 EKWTHDPFSAHKDEDGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEIGGHDGMEKFVKTEEFKKLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 169 AGFALDEGLANPTDAFTVFYSERSPWWIRVTSTGKPGHASRFIEDTAAEKLHKVVNSILAFREKERQRLQANPHLKEGAV 248
Cdd:cd05646 161 VGFALDEGLASPTEEYRVFYGERSPWWVVITAPGTPGHGSKLLENTAGEKLRKVIESIMEFRESQKQRLKSNPNLTLGDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 249 TSVNLTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWCQEAGEGVTFEFAQKFTEPRMTPTDDTDPWWAAFS 328
Cdd:cd05646 241 TTVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEAGRGVTYEFEQKSPEKDPTSLDDSNPWWAAFK 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81884653 329 GACKEMNLTLEPEIFPAATDSRYIRAVGIPALGFSPMNRTPVLLHDHNERLHEAVFLRGVDIYTRLVAALA 399
Cdd:cd05646 321 KAVKEMGLKLKPEIFPAATDSRYIRALGIPALGFSPMNNTPILLHDHNEFLNEDVFLRGIEIYEKIIPALA 391
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
1-401 |
0e+00 |
|
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids.
Pssm-ID: 273850 [Multi-domain] Cd Length: 400 Bit Score: 708.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 1 MTTKGPEsEHPSVTLFRQYLRICTVQPNPDYGSAVTFLEERARQLGLSCQKIEVAPGYVITVLTWPGTNPLLHSILLNSH 80
Cdd:TIGR01880 1 MSSSKWE-EDIAVTRFREYLRINTVQPNPDYAACVDFLIKQADELGLARKTIEFVPGKPVVVLTWPGSNPELPSILLNSH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 81 TDVVPVFKEHWHHDPFEAFKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFVK 160
Cdd:TIGR01880 80 TDVVPVFREHWTHPPFSAFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGGHDGMEKFAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 161 RPEFQALRAGFALDEGLANPTDAFTVFYSERSPWWIRVTSTGKPGHASRFIEDTAAEKLHKVVNSILAFREKERQRLQAN 240
Cdd:TIGR01880 160 TDEFKALNLGFALDEGLASPDDVYRVFYAERVPWWVVVTAPGNPGHGSKLMENTAMEKLEKSVESIRRFRESQFQLLQSN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 241 PHLKEGAVTSVNLTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWCQEAGEGVTFEFAQKFTEPRMTPTDDT 320
Cdd:TIGR01880 240 PDLAIGDVTSVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVDFEEMENRLDEWCADAGEGVTYEFSQHSGKPLVTPHDDS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 321 DPWWAAFSGACKEMNLTLEPEIFPAATDSRYIRAVGIPALGFSPMNRTPVLLHDHNERLHEAVFLRGVDIYTRLVAALAS 400
Cdd:TIGR01880 320 NPWWVAFKDAVKEMGCTFKPEILPGSTDSRYIRAAGVPALGFSPMNNTPVLLHDHNEFLNEAVFLRGIEIYQTLISALAS 399
|
.
gi 81884653 401 V 401
Cdd:TIGR01880 400 V 400
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
13-399 |
4.91e-77 |
|
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440389 [Multi-domain] Cd Length: 388 Bit Score: 243.64 E-value: 4.91e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 13 VTLFRQYLRICTVQPNPDygSAVTFLEERARQLGLSCQKIEVAPGYVITVLTWPGTNPLlHSILLNSHTDVVPV-FKEHW 91
Cdd:COG0624 15 LELLRELVRIPSVSGEEA--AAAELLAELLEALGFEVERLEVPPGRPNLVARRPGDGGG-PTLLLYGHLDVVPPgDLELW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 92 HHDPFEAfKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHkGMELFVKRpEFQALRAGF 171
Cdd:COG0624 92 TSDPFEP-TIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSP-GARALVEE-LAEGLKADA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 172 ALDeglANPTDAFTVFYSERSPWWIRVTSTGKPGHASRFIE-DTAAEKLHKVVNSILAFREKERqrlqANPHLKEgavTS 250
Cdd:COG0624 169 AIV---GEPTGVPTIVTGHKGSLRFELTVRGKAAHSSRPELgVNAIEALARALAALRDLEFDGR----ADPLFGR---TT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 251 VNLTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWCQEAGEG--VTFEFAQKFTEPRMTPTDdtDPWWAAFS 328
Cdd:COG0624 239 LNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGveVEVEVLGDGRPPFETPPD--SPLVAAAR 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81884653 329 GACKE-MNLTLEPEIFPAATDSRYI-RAVGIPALGFSPMNRTpvLLHDHNERLHEAVFLRGVDIYTRLVAALA 399
Cdd:COG0624 317 AAIREvTGKEPVLSGVGGGTDARFFaEALGIPTVVFGPGDGA--GAHAPDEYVELDDLEKGARVLARLLERLA 387
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
76-397 |
2.03e-60 |
|
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 460247 [Multi-domain] Cd Length: 315 Bit Score: 198.34 E-value: 2.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 76 LLNSHTDVVPVfkEHWHHDPFEAFKDseGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRfPRTIHMTFVPDEEvGGHKGM 155
Cdd:pfam01546 1 LLRGHMDVVPD--EETWGWPFKSTED--GKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEE-GGMGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 156 ELFVKRPEFQALRAGFALDEGLANPTD-----AFTVFYSERSPWWIRVTSTGKPGHASRF-IEDTAAEKLHKVVNSILAF 229
Cdd:pfam01546 75 RALIEDGLLEREKVDAVFGLHIGEPTLleggiAIGVVTGHRGSLRFRVTVKGKGGHASTPhLGVNAIVAAARLILALQDI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 230 REKERQRLqanphlkEGAVTSV-NLTKLEGGVayNVVPATMSACFDFRVAPDVDMKAFEKQLQSWCQEAGE--GVTFEFa 306
Cdd:pfam01546 155 VSRNVDPL-------DPAVVTVgNITGIPGGV--NVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAayGVKVEV- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 307 qKFTEPRMTPTDDTDPWWAAFSGACKEM---NLTLEPEIFPAATDSRYIrAVGIPA--LGFSPMNRTpvlLHDHNERLHE 381
Cdd:pfam01546 225 -EYVEGGAPPLVNDSPLVAALREAAKELfglKVELIVSGSMGGTDAAFF-LLGVPPtvVFFGPGSGL---AHSPNEYVDL 299
|
330
....*....|....*.
gi 81884653 382 AVFLRGVDIYTRLVAA 397
Cdd:pfam01546 300 DDLEKGAKVLARLLLK 315
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
13-395 |
1.50e-51 |
|
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group contains proteins that have been uncharacterized to date with similarity to vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis.
Pssm-ID: 349924 [Multi-domain] Cd Length: 431 Bit Score: 178.32 E-value: 1.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 13 VTLFRQYLRICTVQPNPDYGS---AVTFLEERARQLGLS--CQKIEVAPGYVITVLTWPGTNPLLHSILLNSHTDVVPVF 87
Cdd:cd05675 1 VDLLQELIRIDTTNSGDGTGSetrAAEVLAARLAEAGIQteIFVVESHPGRANLVARIGGTDPSAGPLLLLGHIDVVPAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 88 KEHWHHDPFEAfKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFVK-RPE-FQ 165
Cdd:cd05675 81 ASDWSVDPFSG-EIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGENGAKWLVDnHPElFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 166 AlrAGFALDEG------LANPTDAFTVFYSERSPWWIRVTSTGKPGHASRFIEDTAAEKLHKVVNSILAFREKER----- 234
Cdd:cd05675 160 G--ATFALNEGgggslpVGKGRRLYPIQVAEKGIAWMKLTVRGRAGHGSRPTDDNAITRLAEALRRLGAHNFPVRltdet 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 235 --------------------------QRLQA----NPHLKEGAVTSVNLTKLEGGVAYNVVPATMSACFDFRVAPDVDMK 284
Cdd:cd05675 238 ayfaqmaelaggeggalmltavpvldPALAKlgpsAPLLNAMLRNTASPTMLDAGYATNVLPGRATAEVDCRILPGQSEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 285 AFEKQLQswcQEAGE-GVTFEFAQKftEPRMTPTDDTdPWWAAFSGACKEM--NLTLEPEIFPAATDSRYIRAVGIPALG 361
Cdd:cd05675 318 EVLDTLD---KLLGDpDVSVEAVHL--EPATESPLDS-PLVDAMEAAVQAVdpGAPVVPYMSPGGTDAKYFRRLGIPGYG 391
|
410 420 430
....*....|....*....|....*....|....*....
gi 81884653 362 FSPMNRTPVL-----LHDHNERLHEAVFLRGVDIYTRLV 395
Cdd:cd05675 392 FAPLFLPPELdytglFHGVDERVPVESLYFGVRFLDRLV 430
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
15-395 |
3.60e-48 |
|
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE)-like; Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) like family of enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this family are mostly bacterial and have been inferred by homology as being related to both ArgE and DapE. This family also includes N-acetyl-L-citrulline deacetylase (ACDase; acetylcitrulline deacetylase), a unique, novel enzyme found in Xanthomonas campestris, a plant pathogen, in which N-acetyl-L-ornithine is the substrate for transcarbamoylation reaction, and the product is N-acetyl-L-citrulline. Thus, in the arginine biosynthesis pathway, ACDase subsequently catalyzes the hydrolysis of N-acetyl-L-citrulline to acetate and L-citrulline.
Pssm-ID: 349944 [Multi-domain] Cd Length: 361 Bit Score: 167.86 E-value: 3.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 15 LFRQYLRICTVqpNPDYGSAVTFLEE--RARQLGLSCQKIEVAPGYVITVLTwpGTNPLLhsiLLNSHTDVVPVFKEH-W 91
Cdd:cd08659 2 LLQDLVQIPSV--NPPEAEVAEYLAEllAKRGYGIESTIVEGRGNLVATVGG--GDGPVL---LLNGHIDTVPPGDGDkW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 92 HHDPFEAfKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGhKGMELFVKRPefQALRAGF 171
Cdd:cd08659 75 SFPPFSG-RIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGS-DGARALLEAG--YADRLDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 172 ALDeglANPTDaFTVFYSERSPWWIRVTSTGKPGHASRfiEDTAAEKLHKVVNSILAFREkERQRLQANPHLKEgavTSV 251
Cdd:cd08659 151 LIV---GEPTG-LDVVYAHKGSLWLRVTVHGKAAHSSM--PELGVNAIYALADFLAELRT-LFEELPAHPLLGP---PTL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 252 NLTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWCQEAGEGVTFEFAqkFTEPRMTPTDDTDPWWAAFSGAC 331
Cdd:cd08659 221 NVGVINGGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVS--LDGDPPFFTDPDHPLVQALQAAA 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81884653 332 KEMNLTLEPEIFPAATDSRYI-RAVGIPALGFSPMNrtPVLLHDHNERLHEAVFLRGVDIYTRLV 395
Cdd:cd08659 299 RALGGDPVVRPFTGTTDASYFaKDLGFPVVVYGPGD--LALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
13-377 |
6.95e-44 |
|
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences contains annotations for both acetylornithine deacetylase and succinyl-diaminopimelate desuccinylase, but does not contain any members with experimental characterization. Bacillus, Staphylococcus and Sulfolobus species contain multiple hits to this subfamily and each may have a separate activity. Determining which is which must await further laboratory research. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273870 [Multi-domain] Cd Length: 375 Bit Score: 156.79 E-value: 6.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 13 VTLFRQYLRICTVQP-NPDYGSAVTFLEERARQLGLSCQKIEVAPGYVIT----VLTWPGTN--PLLHsilLNSHTDVVP 85
Cdd:TIGR01910 1 VELLKDLISIPSVNPpGGNEETIANYIKDLLREFGFSTDVIEITDDRLKVlgkvVVKEPGNGneKSLI---FNGHYDVVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 86 V-FKEHWHHDPFEAfKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFVKRpef 164
Cdd:TIGR01910 78 AgDLELWKTDPFKP-VEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTLYLLQRG--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 165 qalraGFALDEGL--ANPTDAFTVFYSERSPWWIRVTSTGKPGHASR--FIEDtAAEKLHKVVNSIlafREKERQRLQAN 240
Cdd:TIGR01910 154 -----YFKDADGVliPEPSGGDNIVIGHKGSIWFKLRVKGKQAHASFpqFGVN-AIMKLAKLITEL---NELEEHIYARN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 241 PHLKEGAVTSVNLTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWCQEAG--EGVTFEFAQKFTEPRMTPTD 318
Cdd:TIGR01910 225 SYGFIPGPITFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSksDGWLYENEPVVKWSGPNETP 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81884653 319 DTDPWWAAFSGACKEMnLTLEPEI--FPAATDSRYIRAVGIPALGFSP-MNRTPvllHDHNE 377
Cdd:TIGR01910 305 PDSRLVKALEAIIKKV-RGIEPEVlvSTGGTDARFLRKAGIPSIVYGPgDLETA---HQVNE 362
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
20-400 |
6.12e-42 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 153.95 E-value: 6.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 20 LRICTV--QPNPDYGSA-----VTFLEERARQLGLSCQKIEVApGYVItVLTWPGTNPLLHSILLNSHTDVVPV---FKE 89
Cdd:PRK08262 54 IRFRTIsnRDRAEDDAAafdalHAHLEESYPAVHAALEREVVG-GHSL-LYTWKGSDPSLKPIVLMAHQDVVPVapgTEG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 90 HWHHDPFEAFKDsEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHkGMELFVKRPEFQALRA 169
Cdd:PRK08262 132 DWTHPPFSGVIA-DGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDEEVGGL-GARAIAELLKERGVRL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 170 GFALDEGLANPTDAFTVF--------YSERSPWWIRVTSTGKPGHASRFIEDTAAEKLHKVVNSI------LAFREKERQ 235
Cdd:PRK08262 210 AFVLDEGGAITEGVLPGVkkpvaligVAEKGYATLELTARATGGHSSMPPRQTAIGRLARALTRLednplpMRLRGPVAE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 236 RLQ--------------ANPHLKEGAV---------------TSVNLTKLEGGVAYNVVPATMSACFDFRVAP----DVD 282
Cdd:PRK08262 290 MFDtlapemsfaqrvvlANLWLFEPLLlrvlakspetaamlrTTTAPTMLKGSPKDNVLPQRATATVNFRILPgdsvESV 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 283 MKAFEKQLqswcqeAGEGVTFEFAQKFTEPRmtPTDDTD-PWWAAFSGACKEM--NLTLEPEIFPAATDSRYIRAVGIPA 359
Cdd:PRK08262 370 LAHVRRAV------ADDRVEIEVLGGNSEPS--PVSSTDsAAYKLLAATIREVfpDVVVAPYLVVGATDSRHYSGISDNV 441
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 81884653 360 LGFSPMNRTP---VLLHDHNERLHEAVFLRGVDIYTRLVAALAS 400
Cdd:PRK08262 442 YRFSPLRLSPedlARFHGTNERISVANYARMIRFYYRLIENAAG 485
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
12-400 |
5.07e-41 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 149.37 E-value: 5.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 12 SVTLFRQYLRICTVQPNP-DYGSAVTFLEERARQLGLSCQKIEVAPGYVITVLTWP--------GTNPLLHsilLNSHTD 82
Cdd:PRK08651 8 IVEFLKDLIKIPTVNPPGeNYEEIAEFLRDTLEELGFSTEIIEVPNEYVKKHDGPRpnliarrgSGNPHLH---FNGHYD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 83 VVPVfKEHWH-HDPFEAFKDsEGYIYARGAQDMKS--VSIqyLEAVRRLKSEGhrfPRTIHMTFVPDEEVGGHKGMELfv 159
Cdd:PRK08651 85 VVPP-GEGWSvNVPFEPKVK-DGKVYGRGASDMKGgiAAL--LAAFERLDPAG---DGNIELAIVPDEETGGTGTGYL-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 160 krpefqALRAGFALDEGL-ANPTDAFTVFYSERSPWWIRVTSTGKPGHASR-FIEDTAAEKLHKVVNSILAFREKERQRL 237
Cdd:PRK08651 156 ------VEEGKVTPDYVIvGEPSGLDNICIGHRGLVWGVVKVYGKQAHASTpWLGINAFEAAAKIAERLKSSLSTIKSKY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 238 QANPHlkEGAVTSVNL--TKLEGGVAYNVVPATMSACFDFRVAPDVDM----KAFEKQLQSWCQEAGEGVTFEFAQkFTE 311
Cdd:PRK08651 230 EYDDE--RGAKPTVTLggPTVEGGTKTNIVPGYCAFSIDRRLIPEETAeevrDELEALLDEVAPELGIEVEFEITP-FSE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 312 PRMTPTDdtDPWWAAFSgACKEMNLTLEPE--IFPAATDSRYIRAVGIPALGFSPMNrtPVLLHDHNERLHEAVFLRGVD 389
Cdd:PRK08651 307 AFVTDPD--SELVKALR-EAIREVLGVEPKktISLGGTDARFFGAKGIPTVVYGPGE--LELAHAPDEYVEVKDVEKAAK 381
|
410
....*....|.
gi 81884653 390 IYTRLVAALAS 400
Cdd:PRK08651 382 VYEEVLKRLAK 392
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
27-395 |
5.05e-35 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349933 [Multi-domain] Cd Length: 355 Bit Score: 132.51 E-value: 5.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 27 PNP---DYGSAVTFLEERARQLGLSCQKIEVAPG--YVITVLTWPGTNPllhSILLNSHTDVVPVFKEH-WHHDPFEAfK 100
Cdd:cd08011 13 PNPpgdNTSAIAAYIKLLLEDLGYPVELHEPPEEiyGVVSNIVGGRKGK---RLLFNGHYDVVPAGDGEgWTVDPYSG-K 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 101 DSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKG----MELFVKRPefqalraGFALdeg 176
Cdd:cd08011 89 IKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGtkylLEKVRIKP-------NDVL--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 177 LANPTDAFTVFYSERSPWWIRVTSTGKPGHASRFiedtaaeklHKVVNSIlafrekeRQRLQANPHLKEgAVTSVNLTKL 256
Cdd:cd08011 159 IGEPSGSDNIRIGEKGLVWVIIEITGKPAHGSLP---------HRGESAV-------KAAMKLIERLYE-LEKTVNPGVI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 257 EGGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLQSwCQEAGEGVTFEFAQkftEPRMTPTDDTDPWWAAFSGACKEM-N 335
Cdd:cd08011 222 KGGVKVNLVPDYCEFSVDIRLPPGISTDEVLSRIID-HLDSIEEVSFEIKS---FYSPTVSNPDSEIVKKTEEAITEVlG 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 336 LTLEPEIFPAATDSRYIRAVGIPALGFSPMNrtPVLLHDHNERLHEAVFLRGVDIYTRLV 395
Cdd:cd08011 298 IRPKEVISVGASDARFYRNAGIPAIVYGPGR--LGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
51-395 |
2.75e-33 |
|
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure.
Pssm-ID: 349923 [Multi-domain] Cd Length: 471 Bit Score: 129.68 E-value: 2.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 51 KIEVAPGYVItVLTWPGTNPLLHSILLNSHTDVVPVFKEH---WHHDPFEAFKDsEGYIYARGAQDMKSVSIQYLEAVRR 127
Cdd:cd05674 49 KVEVVNEYGL-LYTWEGSDPSLKPLLLMAHQDVVPVNPETedqWTHPPFSGHYD-GGYIWGRGALDDKNSLIGILEAVEL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 128 LKSEGHRFPRTIHMTFVPDEEVGGHKGMELFVKRPEFQALRAGFA--LDEGLAN-PTDAFTVFY-----SER--SPWWIR 197
Cdd:cd05674 127 LLKRGFKPRRTIILAFGHDEEVGGERGAGAIAELLLERYGVDGLAaiLDEGGAVlEGVFLGVPFalpgvAEKgyMDVEIT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 198 VTSTGkpGHAS-------------------------RFIEDT--------AAEKLHKVVNSILAfrekerQRLQANPHLK 244
Cdd:cd05674 207 VHTPG--GHSSvppkhtgigilseavaaleanpfppKLTPGNpyygmlqcLAEHSPLPPRSLKS------NLWLASPLLK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 245 EGAV---------------TSVNLTKLEGGVAYNVVPATMSACFDFRVAP----------------DVDMK------AFE 287
Cdd:cd05674 279 ALLAsellstspltrallrTTQAVDIINGGVKINALPETATATVNHRIAPgssveevlehvknliaDIAVKyglglsAFG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 288 KQLqswcQEAGEGVTFEFAQKFTEPRMTPTDDTDPwWAAFSGACKEM------NLTLEPEIFPAATDSRYIRAVGIPALG 361
Cdd:cd05674 359 GDV----IYSTNGTKLLTSLLSPEPSPVSSTSSPV-WQLLAGTIRQVfeqfgeDLVVAPGIMTGNTDTRHYWNLTKNIYR 433
|
410 420 430
....*....|....*....|....*....|....*..
gi 81884653 362 FSPMNRTPVLL---HDHNERLHEAVFLRGVDIYTRLV 395
Cdd:cd05674 434 FTPIRLNPEDLgriHGVNERISIDDYLETVAFYYQLI 470
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
34-399 |
2.94e-33 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 129.74 E-value: 2.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 34 AVTFLEERARQLGLSCQKIEVAPGYVIT---VLTWPGTNPLlHSILLNSHTDVVPVFKEHWHHDPFEaFKDSEGYIYARG 110
Cdd:PRK09133 61 AAEAMAARLKAAGFADADIEVTGPYPRKgnlVARLRGTDPK-KPILLLAHMDVVEAKREDWTRDPFK-LVEENGYFYGRG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 111 AQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGME-LFVKRPEfqALRAGFALDEGLANPTD------A 183
Cdd:PRK09133 139 TSDDKADAAIWVATLIRLKREGFKPKRDIILALTGDEEGTPMNGVAwLAENHRD--LIDAEFALNEGGGGTLDedgkpvL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 184 FTVFYSERSPWWIRVTSTGKPGHASRFIEDTAAEKLHKVVNSILAFR--------------------------------- 230
Cdd:PRK09133 217 LTVQAGEKTYADFRLEVTNPGGHSSRPTKDNAIYRLAAALSRLAAYRfpvmlndvtrayfkqsaaietgplaaamrafaa 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 231 ----EKERQRLQANPHLKEGAVTSVNLTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWCQEAGEGVTFEfa 306
Cdd:PRK09133 297 npadEAAIALLSADPSYNAMLRTTCVATMLEGGHAENALPQRATANVNCRIFPGDTIEAVRATLKQVVADPAIKITRI-- 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 307 qkfTEPRMTPTDDTDP-WWAAFSGACKEM--NLTLEPEIFPAATDSRYIRAVGIPALGFSPM--NRTPVLLHDHNERLHE 381
Cdd:PRK09133 375 ---GDPSPSPASPLRPdIMKAVEKLTAAMwpGVPVIPSMSTGATDGRYLRAAGIPTYGVSGLfgDPDDTFAHGLNERIPV 451
|
410
....*....|....*...
gi 81884653 382 AVFLRGVDIYTRLVAALA 399
Cdd:PRK09133 452 ASFYEGRDFLYELVKDLA 469
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
13-369 |
1.05e-32 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 127.66 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 13 VTLFRQYLRICTVQPNPDYGS----AVTFLEERARQLGLSCQKIEVAPGYVITVLTWPGTNPLLHSILLNSHTDVVPVFK 88
Cdd:PRK07906 2 VDLCSELIRIDTTNTGDGTGKgereAAEYVAEKLAEVGLEPTYLESAPGRANVVARLPGADPSRPALLVHGHLDVVPAEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 89 EHWHHDPFE-AFKDseGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFV-KRPE-FQ 165
Cdd:PRK07906 82 ADWSVHPFSgEIRD--GYVWGRGAVDMKDMDAMMLAVVRHLARTGRRPPRDLVFAFVADEEAGGTYGAHWLVdNHPElFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 166 ALRA------GFALDegLANPTDAFTVFYSERSPWWIRVTSTGKPGHASRFIEDTAAEKLHKVVNSILAFR------EKE 233
Cdd:PRK07906 160 GVTEaisevgGFSLT--VPGRDRLYLIETAEKGLAWMRLTARGRAGHGSMVNDDNAVTRLAEAVARIGRHRwplvltPTV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 234 RQRLQA------------NPHL---KEGAV---------TSVNLTKLEGGVAYNVVPATMSACFDFRVAPDVDmKAFEKQ 289
Cdd:PRK07906 238 RAFLDGvaeltglefdpdDPDAllaKLGPAarmvgatlrNTANPTMLKAGYKVNVIPGTAEAVVDGRFLPGRE-EEFLAT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 290 LQSWcqeAGEGVTFEFAQkfteprmtptdDTDPWWAAFSGACKE-MNLTLE---------PEIFPAATDSRYIRAVGIPA 359
Cdd:PRK07906 317 VDEL---LGPDVEREWVH-----------RDPALETPFDGPLVDaMNAALLaedpgarvvPYMLSGGTDAKAFSRLGIRC 382
|
410
....*....|
gi 81884653 360 LGFSPMnRTP 369
Cdd:PRK07906 383 YGFAPL-RLP 391
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
37-365 |
2.29e-29 |
|
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, Glutamate carboxypeptidase (carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; CPDG2; CPG2; Folate hydrolase G2; Pteroylmonoglutamic acid hydrolase G2; Glucarpidase; E.C. 3.4.17.11) subfamily. CPDG2 is a periplasmic enzyme that is synthesized with a signal peptide. It is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. CPDG2 cleaves the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl, and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolyzing it to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy; for example, glutamate can be cleaved from glutamated benzoyl nitrogen mustards, producing nitrogen mustards with effective cytotoxicity against tumor cells.
Pssm-ID: 349881 [Multi-domain] Cd Length: 362 Bit Score: 116.92 E-value: 2.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 37 FLEERARQLGLSCQKIEVAPGYVITVLTWPGTNPLlhSILLNSHTDVVpvfkehWHHD--PFEAFKDSEGYIYARGAQDM 114
Cdd:cd03885 27 LLAEELEALGFTVERRPLGEFGDHLIATFKGTGGK--RVLLIGHMDTV------FPEGtlAFRPFTVDGDRAYGPGVADM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 115 KSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFVKrpefQALRAGFALDEGLANPTDAFTVFYSERSPW 194
Cdd:cd03885 99 KGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGSRELIEE----EAKGADYVLVFEPARADGNLVTARKGIGRF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 195 WIRVtsTGKPGHASRFIEDTAAeklhkvvnsilAFREKERQRLQANPHLKEGAVTSVNLTKLEGGVAYNVVPATMSACFD 274
Cdd:cd03885 175 RLTV--KGRAAHAGNAPEKGRS-----------AIYELAHQVLALHALTDPEKGTTVNVGVISGGTRVNVVPDHAEAQVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 275 FRVAPDVDMKAFEKQLQSWCQEA-GEGVTFEFAQKFTEPRMTPTDDTDPWWAAFSGACKEMNLTLEPEIFPAATDSRYIR 353
Cdd:cd03885 242 VRFATAEEADRVEEALRAIVATTlVPGTSVELTGGLNRPPMEETPASRRLLARAQEIAAELGLTLDWEATGGGSDANFTA 321
|
330
....*....|...
gi 81884653 354 AVGIPAL-GFSPM 365
Cdd:cd03885 322 ALGVPTLdGLGPV 334
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
24-396 |
1.27e-28 |
|
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16) subfamily. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349889 [Multi-domain] Cd Length: 367 Bit Score: 115.00 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 24 TVQPNPDyGSAVTFLEERARQLGLSCQKIEVAPG----YVITVLtwPGTNPllhSILLNSHTDVVPVFKEHWHHDPFEAf 99
Cdd:cd03894 11 TVSRNSN-LALIEYVADYLAALGVKSRRVPVPEGgkanLLATLG--PGGEG---GLLLSGHTDVVPVDGQKWSSDPFTL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 100 KDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPrtIHMTFVPDEEVGgHKGMELFVKRPEFQALRAGFALdegLAN 179
Cdd:cd03894 84 TERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKP--LHLAFSYDEEVG-CLGVRHLIAALAARGGRPDAAI---VGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 180 PTD-AFTVFYSERSPWWIRVTstGKPGHASrfieDT-----AAEKLHKVVNSILAFREKERQRLqANPHLKEGAVTsVNL 253
Cdd:cd03894 158 PTSlQPVVAHKGIASYRIRVR--GRAAHSS----LPplgvnAIEAAARLIGKLRELADRLAPGL-RDPPFDPPYPT-LNV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 254 TKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWCQEAGE----GVTFEfaqKFTEPRMTPTDDTDPWWAAFSG 329
Cdd:cd03894 230 GLIHGGNAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEfpeaGIEVE---PLFEVPGLETDEDAPLVRLAAA 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81884653 330 ACKEMNltlePEIFPAATDSRYIRAVGIPALGFSP--MNRTpvllHDHNERLHEAVFLRGVDIYTRLVA 396
Cdd:cd03894 307 LAGDNK----VRTVAYGTEAGLFQRAGIPTVVCGPgsIAQA----HTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
62-391 |
1.79e-27 |
|
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349870 [Multi-domain] Cd Length: 200 Bit Score: 107.90 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 62 VLTWPGTNPLlHSILLNSHTDVVPVFKEHWHHDPFEAFKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHM 141
Cdd:cd03873 3 IARLGGGEGG-KSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 142 TFVPDEEVGGHKGMELFVKrpefQALRAGFALDEglanptdaftVFYSERSPWWIrvtstGKPGHASRFiedtaaeklhk 221
Cdd:cd03873 82 AFTADEEVGSGGGKGLLSK----FLLAEDLKVDA----------AFVIDATAGPI-----LQKGVVIRN----------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 222 vvnsilafrekerqrlqanphlkegavtsvnltkleggvaynvvpatmsacfdfrvapdvdmkafekqlqswcqeagegv 301
Cdd:cd03873 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 302 tfefaqkfteprmtptddtdPWWAAFSGACKEMNLTL-EPEIFPAATDSRYIRAVGIPALGFSPMnrTPVLLHDHNERLH 380
Cdd:cd03873 132 --------------------PLVDALRKAAREVGGKPqRASVIGGGTDGRLFAELGIPGVTLGPP--GDKGAHSPNEFLN 189
|
330
....*....|.
gi 81884653 381 EAVFLRGVDIY 391
Cdd:cd03873 190 LDDLEKATKVY 200
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
62-391 |
3.09e-25 |
|
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349948 [Multi-domain] Cd Length: 198 Bit Score: 101.74 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 62 VLTWPGTnPLLHSILLNSHTDVVPVFKEHWHHDPFEAFKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHM 141
Cdd:cd18669 3 IARYGGG-GGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 142 TFVPDEEVGGHKGMELFVKRpefqALRAGFALDEglanptdaftVFYSERSPWWirvtstgKPGHASRFiedtaaeklhk 221
Cdd:cd18669 82 AFTPDEEVGSGAGKGLLSKD----ALEEDLKVDY----------LFVGDATPAP-------QKGVGIRT----------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 222 vvnsilafrekerqrlqanphlkegavtsvnltkleggvaynvvpatmsacfdfrvapdvdmkafekqlqswcqeagegv 301
Cdd:cd18669 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 302 tfefaqkfteprmtptddtdPWWAAFSGACKEMNLTLEPEI-FPAATDSRYIRAVGIPALGFSPMnrTPVLLHDHNERLH 380
Cdd:cd18669 130 --------------------PLVDALSEAARKVFGKPQHAEgTGGGTDGRYLQELGIPGVTLGAG--GGKGAHSPNERVN 187
|
330
....*....|.
gi 81884653 381 EAVFLRGVDIY 391
Cdd:cd18669 188 LEDLESALAVL 198
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
32-380 |
4.81e-25 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349890 [Multi-domain] Cd Length: 400 Bit Score: 105.47 E-value: 4.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 32 GSAVTFLEERARQLGL-------SCQKIEVAPGYV----------ITVLTWPGTNPLLHSILLNSHTDVVPVFK-EHWHH 93
Cdd:cd03895 17 AAAQDLVAAALRSRGYtvdrweiDVEKLKHHPGFSpvavdyagapNVVGTHRPRGETGRSLILNGHIDVVPEGPvELWTR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 94 DPFEAfKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMelfvkrpefQALRAGFAL 173
Cdd:cd03895 97 PPFEA-TIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEECTGNGAL---------AALMRGYRA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 174 DEGLANPTDAFTVFYSERSPWWIRVTSTGKPGHASRFIEDTAA-EKLHKVVNSILAFREKERQRLQANPHL--KEGAVTs 250
Cdd:cd03895 167 DAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAiEKAMHLIQALQELEREWNARKKSHPHFsdHPHPIN- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 251 VNLTKLEGGVAYNVVPATMSacFDFRVA--PDVDMKAFEKQLQSWCQEA--------GEGVTFEFAQKFTEPRMTPtdDT 320
Cdd:cd03895 246 FNIGKIEGGDWPSSVPAWCV--LDCRIGiyPGESPEEARREIEECVADAaatdpwlsNHPPEVEWNGFQAEGYVLE--PG 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81884653 321 DPWWAAFSGACKEM-NLTLEPEIFPAATDSR-YIRAVGIPALGFSPMNRTPvllHDHNERLH 380
Cdd:cd03895 322 SDAEQVLAAAHQAVfGTPPVQSAMTATTDGRfFVLYGDIPALCYGPGSRDA---HGFDESVD 380
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
13-394 |
1.48e-21 |
|
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE; aspartyl dipeptidase; succinyl-diaminopimelate desuccinylase) subfamily. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from Escherichia coli and Haemophilus influenzae, while the genes that encode for DapEs have been sequenced from several bacterial sources such as Corynebacterium glutamicum, Helicobacter pylori, Neisseria meningitidis and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme that requires two zinc atoms per molecule for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349886 [Multi-domain] Cd Length: 366 Bit Score: 94.88 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 13 VTLFRQYLRICTVQPNpDYGsAVTFLEERARQLGLSCQKIEVapGYVITVLTWPGTNPLLhsILLNSHTDVVPV-FKEHW 91
Cdd:cd03891 1 LELAKELIRRPSVTPD-DAG-AQDLIAERLKALGFTCERLEF--GGVKNLWARRGTGGPH--LCFAGHTDVVPPgDLEGW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 92 HHDPFEAfKDSEGYIYARGAQDMKSvSIQ-YLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFVKRPEFQALRAG 170
Cdd:cd03891 75 SSDPFSP-TIKDGMLYGRGAADMKG-GIAaFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGTKKVLEWLKARGEKID 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 171 FALdegLANPT------DAftvfyserspwwIRV----------TSTGKPGHASrfIEDTAAEKLHKVVNSILAFreker 234
Cdd:cd03891 153 YCI---VGEPTsekklgDT------------IKIgrrgslngklTIKGKQGHVA--YPHLADNPIHLLAPILAEL----- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 235 qrlqANPHLKEG----AVTSVNLTKLEGGV-AYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWCQEAGEGVTFEFAQKf 309
Cdd:cd03891 211 ----TATVLDEGneffPPSSLQITNIDVGNgATNVIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLDYDLEWKLS- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 310 TEPRMTPTDD-TDpwwaAFSGACKEmNLTLEPEIfpaAT-----DSRYIRAVGIPALGFSPMNRTpvlLHDHNERLHEAV 383
Cdd:cd03891 286 GEPFLTKPGKlVD----AVSAAIKE-VTGITPEL---STsggtsDARFIASYGCPVVEFGLVNAT---IHKVNERVSVAD 354
|
410
....*....|.
gi 81884653 384 FLRGVDIYTRL 394
Cdd:cd03891 355 LEKLTDIYERI 365
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
74-396 |
5.19e-19 |
|
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. These hypothetical proteins have been inferred by homology to be exopeptidases: carboxypeptidases, dipeptidases and a specialized aminopeptidase. In general, the peptidase hydrolyzes the late products of protein degradation in order to complete the conversion of proteins to free amino acids. Members of this subfamily may bind metal ions such as zinc.
Pssm-ID: 349869 [Multi-domain] Cd Length: 394 Bit Score: 88.00 E-value: 5.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 74 SILLNSHTDVVPVfKEHWHHDPFEAFKDsEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHK 153
Cdd:cd02697 75 TVALNAHGDVVPP-GDGWTRDPYGAVVE-DGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGGEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 154 GmelfvkrpefqalrAGFALDEGLANPTDA------FTVFYSERSPWWIRVTSTGKPGHASrfIEDTAAEKLH---KVVN 224
Cdd:cd02697 153 G--------------PGWLLRQGLTKPDLLiaagfsYEVVTAHNGCLQMEVTVHGKQAHAA--IPDTGVDALQgavAILN 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 225 SILAFREKERQRLQANPHLKEgavTSVNLTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWCQEAGE---GV 301
Cdd:cd02697 217 ALYALNAQYRQVSSQVEGITH---PYLNVGRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIADAAAsmpGI 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 302 TFEFAQKFTEPRMTPTDDTDPWWAAFSGACKEMNLTLEPEI-FPAATDSRYIRAVGIPALGFSPMNRTpvLLHDHNERLH 380
Cdd:cd02697 294 SVDIRRLLLANSMRPLPGNAPLVEAIQTHGEAVFGEPVPAMgTPLYTDVRLYAEAGIPGVIYGAGPRT--VLESHAKRAD 371
|
330
....*....|....*.
gi 81884653 381 EAVFLRGVDIYTRLVA 396
Cdd:cd02697 372 ERLQLEDLRRATKVIA 387
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
75-395 |
1.46e-18 |
|
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine deacetylases from proteobacteria. This enzyme is the final step of the "acetylated" ornithine biosynthesis pathway. The enzyme is closely related to dapE, succinyl-diaminopimelate desuccinylase, and outside of this clade annotation is very inaccurate as to which function should be ascribed to genes. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130947 [Multi-domain] Cd Length: 364 Bit Score: 86.41 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 75 ILLNSHTDVVPVFKEHWHHDPFEaFKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPrtIHMTFVPDEEVgGHKG 154
Cdd:TIGR01892 61 LALSGHTDVVPYDDAAWTRDPFR-LTEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLKKP--LHLALTADEEV-GCTG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 155 MELFVKRpefQALRAGFALdegLANPTDAFTVfYSERSPWWIRVTSTGKPGHASRfiEDTAAEKLHkVVNSILAFREKER 234
Cdd:TIGR01892 137 APKMIEA---GAGRPRHAI---IGEPTRLIPV-RAHKGYASAEVTVRGRSGHSSY--PDSGVNAIF-RAGRFLQRLVHLA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 235 QRLQANPHLK--EGAVTSVNLTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWCQEAGEGvTFEFAQKFTEP 312
Cdd:TIGR01892 207 DTLLREDLDEgfTPPYTTLNIGVIQGGKAVNIIPGACEFVFEWRPIPGMDPEELLQLLETIAQALVRD-EPGFEVQIEVV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 313 RMTPTDDTDPwwAAFSGACKEMNLTLEPEIFPAATDSRYIRAVGIPALGFSP--MNRTpvllHDHNERLHEAVFLRGVDI 390
Cdd:TIGR01892 286 STDPGVNTEP--DAELVAFLEELSGNAPEVVSYGTEAPQFQELGAEAVVCGPgdIRQA----HQPDEYVEIEDLVRCRAV 359
|
....*
gi 81884653 391 YTRLV 395
Cdd:TIGR01892 360 LARLV 364
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
60-380 |
7.54e-18 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 84.67 E-value: 7.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 60 ITVLTWPGTNPLLHSILLNSHTDVVPVFK-EHWHHDPFEAfKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRT 138
Cdd:PRK06837 85 NVVGTYRPAGKTGRSLILQGHIDVVPEGPlDLWSRPPFDP-VIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPAAR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 139 IHMTFVPDEEVGGHKGMelfvkrpefQALRAGFALDEGL-ANPTDAfTVFYSERSPWWIRVTSTGKPGHASRfiEDTAAE 217
Cdd:PRK06837 164 VHFQSVIEEESTGNGAL---------STLQRGYRADACLiPEPTGE-KLVRAQVGVIWFRLRVRGAPVHVRE--AGTGAN 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 218 KLHKVVNSILAFREKER---QRLQANPHLKEGA-VTSVNLTKLEGGVAYNVVPATmsaC-FDFRVA--PDVDMKAFEKQL 290
Cdd:PRK06837 232 AIDAAYHLIQALRELEAewnARKASDPHFEDVPhPINFNVGIIKGGDWASSVPAW---CdLDCRIAiyPGVTAADAQAEI 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 291 QSWCQEAGEGVTF--------EFAQKFTEP-RMTPTDD-----TDPWWAAFSGAckemnltLEPEIFPAATDSR-YIRAV 355
Cdd:PRK06837 309 EACLAAAARDDRFlsnnppevVWSGFLAEGyVLEPGSEaeaalARAHAAVFGGP-------LRSFVTTAYTDTRfYGLYY 381
|
330 340
....*....|....*....|....*
gi 81884653 356 GIPALGFSPMNRTPvllHDHNERLH 380
Cdd:PRK06837 382 GIPALCYGPSGEGI---HGFDERVD 403
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
70-393 |
9.43e-18 |
|
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, actinobacterial dapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) subfamily. This group is composed of predominantly actinobacterial DapE proteins. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from proteobacteria such as Escherichia coli and Haemophilus influenzae, while genes that encode for DapEs have been sequenced from several bacterial sources such as the actinobacteria Corynebacterium glutamicum and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme (41.6 kDa per subunit) that requires 2 atoms of zinc per molecule of polypeptide for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349899 [Multi-domain] Cd Length: 347 Bit Score: 83.65 E-value: 9.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 70 PLLHSILLNSHTDVVPVfkehwhHDPFEAFKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTihMTFVPDEEV 149
Cdd:cd05647 51 GLASRVILAGHLDTVPV------AGNLPSRVEEDGVLYGCGATDMKAGDAVQLKLAATLAAATLKHDLT--LIFYDCEEV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 150 GGHK-GME-LFVKRPEFqaLRAGFALdegLANPTDAfTVFYSERSPWWIRVTSTGKPGHASR-FIEDTAAEKLHKVVNSI 226
Cdd:cd05647 123 AAELnGLGrLAEEHPEW--LAADFAV---LGEPTDG-TIEGGCQGTLRFKVTTHGVRAHSARsWLGENAIHKLAPILARL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 227 LAFREKE--------RQRLqanphlkegavtsvNLTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLqswcQEAG 298
Cdd:cd05647 197 AAYEPRTvnidgltyREGL--------------NAVFISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHV----REVF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 299 EGVTFEFAQKFTEPRMTPTDDTdPWWAAFSGACKEmnltlEPEIFPAATDSRYIRAVGIPALGFSPMNrtPVLLHDHNER 378
Cdd:cd05647 259 EGLGYEIEVTDLSPGALPGLDH-PVARDLIEAVGG-----KVRAKYGWTDVARFSALGIPAVNFGPGD--PLLAHKRDEQ 330
|
330
....*....|....*
gi 81884653 379 LHEAVFLRGVDIYTR 393
Cdd:cd05647 331 VPVEQITACAAILRR 345
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
28-359 |
2.58e-17 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 82.97 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 28 NPDYG-----SAVTFLEERARQLGLScqKIEV--APG-YVIT------VLTWPGTNP--LLHSIllnSHTDVVPVFKEH- 90
Cdd:PRK13983 21 NPDFGgegekEKAEYLESLLKEYGFD--EVERydAPDpRVIEgvrpniVAKIPGGDGkrTLWII---SHMDVVPPGDLSl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 91 WHHDPFEA-FKDseGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFVKRpefqalra 169
Cdd:PRK13983 96 WETDPFKPvVKD--GKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEETGSKYGIQYLLKK-------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 170 gfalDEGLANPTDAFTV---------F--YSERSPWWIRVTSTGKPGHASRfiedtaaekLHKVVNS-------ILAFRE 231
Cdd:PRK13983 166 ----HPELFKKDDLILVpdagnpdgsFieIAEKSILWLKFTVKGKQCHAST---------PENGINAhraaadfALELDE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 232 KERQRLQANPHLKEGAVTSVNLTKLEGGV-AYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWC----QEAGEGVTFEFA 306
Cdd:PRK13983 233 ALHEKFNAKDPLFDPPYSTFEPTKKEANVdNINTIPGRDVFYFDCRVLPDYDLDEVLKDIKEIAdefeEEYGVKIEVEIV 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 81884653 307 QKFTEPrmTPTDDTDPWWAAFSGACKEMnLTLEPEI--FPAATDSRYIRAVGIPA 359
Cdd:PRK13983 313 QREQAP--PPTPPDSEIVKKLKRAIKEV-RGIEPKVggIGGGTVAAFLRKKGYPA 364
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
13-259 |
3.04e-17 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 82.89 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 13 VTLFRQYLRICTVQPNPD-YGSAVTFLEERARQLGLSCQKI--EVAPGYVITVLTW--------PGTNPLLHsilLNSHT 81
Cdd:PRK13013 17 VALTQDLIRIPTLNPPGRaYREICEFLAARLAPRGFEVELIraEGAPGDSETYPRWnlvarrqgARDGDCVH---FNSHH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 82 DVVPVfKEHWHHDPFEAFKDsEGYIYARGAQDMK---SVSIQYLEAVRRlksEGHRFPRTIHMTFVPDEEVGGHKGMELF 158
Cdd:PRK13013 94 DVVEV-GHGWTRDPFGGEVK-DGRIYGRGACDMKgglAASIIAAEAFLA---VYPDFAGSIEISGTADEESGGFGGVAYL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 159 VKRPEFQALRAGFALdegLANPTDAFTVFYSERSPWWIRVTSTGKPGHASR-FIEDTAAEKLHKVVNsilAFREKERQRL 237
Cdd:PRK13013 169 AEQGRFSPDRVQHVI---IPEPLNKDRICLGHRGVWWAEVETRGRIAHGSMpFLGDSAIRHMGAVLA---EIEERLFPLL 242
|
250 260
....*....|....*....|....*..
gi 81884653 238 Q----ANPHLKEGAVTS-VNLTKLEGG 259
Cdd:PRK13013 243 AtrrtAMPVVPEGARQStLNINSIHGG 269
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
37-282 |
1.74e-16 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal, and have been inferred by similarity as being related to both ArgE and DapE.
Pssm-ID: 349903 [Multi-domain] Cd Length: 340 Bit Score: 80.01 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 37 FLEERARQLGLSCQKIEVAPGYVITVLTWPGTNPLLHsILLNSHTDVVPVFKehwhhdPFEAfKDSEGYIYARGAQDMK- 115
Cdd:cd05652 24 FLAEYLESLGFTVEKQPVENKDRFNVYAYPGSSRQPR-VLLTSHIDTVPPFI------PYSI-SDGGDTIYGRGSVDAKg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 116 SVSIQYLeAVRRLKSEGHRFPRTIHMTFVPDEEVGGHkGM----ELFVKRPEfqALRAGFALDEGLANPTDAFTVFyser 191
Cdd:cd05652 96 SVAAQII-AVEELLAEGEVPEGDLGLLFVVGEETGGD-GMkafnDLGLNTWD--AVIFGEPTELKLASGHKGMLGF---- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 192 spwwiRVTSTGKPGHaSRFIE------DTAAEKLHKVVNSILAFREkerqrlqanphlKEGAvTSVNLTKLEGGVAYNVV 265
Cdd:cd05652 168 -----KLTAKGKAGH-SGYPWlgisaiEILVEALVKLIDADLPSSE------------LLGP-TTLNIGRISGGVAANVV 228
|
250
....*....|....*..
gi 81884653 266 PATMSACFDFRVAPDVD 282
Cdd:cd05652 229 PAAAEASVAIRLAAGPP 245
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
12-398 |
4.10e-16 |
|
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 162269 [Multi-domain] Cd Length: 370 Bit Score: 79.00 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 12 SVTLFRQYLRICTVQPNpDYGsAVTFLEERARQLGLSCQKIEVapGYVITVLTWPGTNPLLhsILLNSHTDVVPV-FKEH 90
Cdd:TIGR01246 1 VTELAKELISRPSVTPN-DAG-CQDIIAERLEKLGFEIEWMHF--GDTKNLWATRGTGEPV--LAFAGHTDVVPAgPEEQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 91 WHHDPFEaFKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFVKRPEFQALRAG 170
Cdd:TIGR01246 75 WSSPPFE-PVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTAIDGTKKVVETLMARDELID 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 171 FALdegLANPTDAF----TVFYSERSPWWIRVTSTGKPGHASrfIEDTAAEKLHKVVNSILAFrekerqrlqANPHLKEG 246
Cdd:TIGR01246 154 YCI---VGEPSSVKklgdVIKNGRRGSITGNLTIKGIQGHVA--YPHLANNPIHKAAPALAEL---------TAIKWDEG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 247 AV----TSVNLTKLEGGV-AYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWCQEAGEGVTFEFAQKfTEPRMTPTDD-T 320
Cdd:TIGR01246 220 NEffppTSLQITNIHAGTgANNVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDYDLEWSLS-GEPFLTNDGKlI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 321 DPWWAAFSGACKEmnltlEPEIFPAA--TDSRYIRAVGIPALGFSPMNRTpvlLHDHNERLHEAVFLRGVDIYTRLVAAL 398
Cdd:TIGR01246 299 DKAREAIEETNGI-----KPELSTGGgtSDGRFIALMGAEVVEFGPVNAT---IHKVNECVSIEDLEKLSDVYQDLLENL 370
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
80-395 |
4.38e-16 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 79.16 E-value: 4.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 80 HTDVVPVFKEH-WHHDPFEAfKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHkGMELF 158
Cdd:PRK08588 67 HMDVVAAGDVDkWTYDPFEL-TEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNGTIRLLATAGEEVGEL-GAKQL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 159 VKrpefqalrAGFALD-EGL--ANPTDAFtVFYSERSPWWIRVTSTGKPGHASrfiedtAAEKLHKVVNSILAFREKERQ 235
Cdd:PRK08588 145 TE--------KGYADDlDALiiGEPSGHG-IVYAHKGSMDYKVTSTGKAAHSS------MPELGVNAIDPLLEFYNEQKE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 236 RL----QANPHLkeGAVTSVNlTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWC----QEAGEGVTFEFAQ 307
Cdd:PRK08588 210 YFdsikKHNPYL--GGLTHVV-TIINGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIInevnQNGAAQLSLDIYS 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 308 KFtEPRMTpTDDTDPWWAAFSGACKEMNLTLEPEIFPAATDSRYIRAVG--IPALGFSP-MNRTPvllHDHNERLHEAVF 384
Cdd:PRK08588 287 NH-RPVAS-DKDSKLVQLAKDVAKSYVGQDIPLSAIPGATDASSFLKKKpdFPVIIFGPgNNLTA---HQVDEYVEKDMY 361
|
330
....*....|.
gi 81884653 385 LRGVDIYTRLV 395
Cdd:PRK08588 362 LKFIDIYKEII 372
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
13-318 |
5.01e-16 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349901 [Multi-domain] Cd Length: 389 Bit Score: 79.04 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 13 VTLFRQYLRICTVqpNPDYG-----SAVTFLEERARQLGLS-CQKIEVAPGYVI----TVLTWPGTNP-LLHSIllnSHT 81
Cdd:cd05650 4 IELERDLIRIPAV--NPESGgegekEKADYLEKKLREYGFYtLERYDAPDERGIirpnIVAKIPGGNDkTLWII---SHL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 82 DVVPVFK-EHWHHDPFEAFKDsEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGME-LFV 159
Cdd:cd05650 79 DTVPPGDlSLWETDPWEPVVK-DGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDGSEYGIQyLLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 160 KRPEFQALRAGFALDEGlaNPTDAFtVFYSERSPWWIRVTSTGKPGHASRfiEDTAAEKLHKVVNSILAFREKERQRLQA 239
Cdd:cd05650 158 KFDLFKKDDLIIVPDFG--TEDGEF-IEIAEKSILWIKVNVKGKQCHAST--PENGINAFVAASNFALELDELLHEKFDE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 240 NPHLKEGAVTSVNLTKLEGGVA-YNVVPATMSACFDFRVAP--DVD--MKAFEKQLQSWCQEAGEGVTFEFAQKFTEPRM 314
Cdd:cd05650 233 KDDLFNPPYSTFEPTKKEANVPnVNTIPGYDVFYFDCRVLPtyKLDevLKFVNKIISDFENSYGAGITYEIVQKEQAPPA 312
|
....
gi 81884653 315 TPTD 318
Cdd:cd05650 313 TPED 316
|
|
| PRK06915 |
PRK06915 |
peptidase; |
74-299 |
5.10e-16 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 79.35 E-value: 5.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 74 SILLNSHTDVVPVFK-EHWHHDPFEAfKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGH 152
Cdd:PRK06915 95 SMILNGHIDVVPEGDvNQWDHHPYSG-EVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEESGGA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 153 KGMelfvkrpefQALRAGFALDEGL-ANPTDaFTVFYSERSPWWIRVTSTGKPGH-ASRFIEDTAAEKLHKVVNSILAFR 230
Cdd:PRK06915 174 GTL---------AAILRGYKADGAIiPEPTN-MKFFPKQQGSMWFRLHVKGKAAHgGTRYEGVSAIEKSMFVIDHLRKLE 243
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 231 EKERQRLqANPHLKEGAV-TSVNLTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWCQEAGE 299
Cdd:PRK06915 244 EKRNDRI-TDPLYKGIPIpIPINIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKEEFENWIAELND 312
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
74-395 |
6.28e-16 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349902 [Multi-domain] Cd Length: 341 Bit Score: 78.12 E-value: 6.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 74 SILLNSHTDVVPVFKEhWHHDPFEAfKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGhrfPRTIHMTFV--PDEEVGG 151
Cdd:cd05651 57 TLLLNSHHDTVKPNAG-WTKDPFEP-VEKGGKLYGLGSNDAGASVVSLLATFLHLYSEG---PLNYNLIYAasAEEEISG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 152 HKGME-LFVKRPEFQALRAGfaldeglaNPTDaFTVFYSERSPWWIRVTSTGKPGHASRFIEDTAaekLHKVVNSILAFR 230
Cdd:cd05651 132 KNGIEsLLPHLPPLDLAIVG--------EPTE-MQPAIAEKGLLVLDCTARGKAGHAARNEGDNA---IYKALDDIQWLR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 231 EKERQRlqANPHLkeGAVTsVNLTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWCQEAGEGVTFEFAQKFT 310
Cdd:cd05651 200 DFRFDK--VSPLL--GPVK-MTVTQINAGTQHNVVPDSCTFVVDIRTTEAYTNEEIFEIIRGNLKSEIKPRSFRLNSSAI 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 311 EPRmtptddtdpwwAAFSGACKEMNLTlePEIFPAATDSRYIravGIPA--LGFSPMNRTpvllHDHNERLHEAVFLRGV 388
Cdd:cd05651 275 PPD-----------HPIVQAAIAAGRT--PFGSPTLSDQALM---PFPSvkIGPGDSSRS----HTADEFIELSEIEEGI 334
|
....*..
gi 81884653 389 DIYTRLV 395
Cdd:cd05651 335 DIYIELL 341
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
34-150 |
1.69e-14 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 74.69 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 34 AVTFLEERARQLGLSCQKIEVAPGYVITVLTWPGTNPLLH-SILLNSHTDVVPVFK-EHWHHDPFEAFKDsEGYIYARGA 111
Cdd:PRK08596 38 AQEFIAEFLRKLGFSVDKWDVYPNDPNVVGVKKGTESDAYkSLIINGHMDVAEVSAdEAWETNPFEPTIK-DGWLYGRGA 116
|
90 100 110
....*....|....*....|....*....|....*....
gi 81884653 112 QDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVG 150
Cdd:PRK08596 117 ADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEVG 155
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
75-296 |
6.72e-14 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 72.53 E-value: 6.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 75 ILLNSHTDVVPVFKEHWHHDPFEAFKDsEGYIYARGAQDMK----SVsiqyLEAVRRLKSEGHRFPrtIHMTFVPDEEVG 150
Cdd:PRK07522 67 IVLSGHTDVVPVDGQAWTSDPFRLTER-DGRLYGRGTCDMKgfiaAA----LAAVPELAAAPLRRP--LHLAFSYDEEVG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 151 --------------GHKGMELFVKRP-EFQALRA--GFAldeglanptdAFtvfyserspwwiRVTSTGKPGHASRfied 213
Cdd:PRK07522 140 clgvpsmiarlperGVKPAGCIVGEPtSMRPVVGhkGKA----------AY------------RCTVRGRAAHSSL---- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 214 taaekLHKVVNSI------LAFREKERQRLQANPHLKEG---AVTSVNLTKLEGGVAYNVVPATMSACFDFRVAPDVDMK 284
Cdd:PRK07522 194 -----APQGVNAIeyaarlIAHLRDLADRLAAPGPFDALfdpPYSTLQTGTIQGGTALNIVPAECEFDFEFRNLPGDDPE 268
|
250
....*....|..
gi 81884653 285 AFEKQLQSWCQE 296
Cdd:PRK07522 269 AILARIRAYAEA 280
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
11-116 |
4.51e-13 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 70.11 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 11 PSVTlfrqylrictvqpnPDYGSAVTFLEERARQLGLSCQKIEVAPgyvITVL--TWPGTNPLLhsiLLNSHTDVVPV-F 87
Cdd:PRK13009 15 PSVT--------------PDDAGCQDLLAERLEALGFTCERMDFGD---VKNLwaRRGTEGPHL---CFAGHTDVVPPgD 74
|
90 100
....*....|....*....|....*....
gi 81884653 88 KEHWHHDPFEAfKDSEGYIYARGAQDMKS 116
Cdd:PRK13009 75 LEAWTSPPFEP-TIRDGMLYGRGAADMKG 102
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
20-398 |
1.25e-12 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 68.87 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 20 LRICTVQPNPDYGS----AVTFLEERARQLGLSCQKIEVAPGYVITVLTWPGTnPLLHSILLNSHTDVVPVFKEH-WHHD 94
Cdd:cd05680 8 LRIPSVSADPAHKGdvrrAAEWLADKLTEAGFEHTEVLPTGGHPLVYAEWLGA-PGAPTVLVYGHYDVQPPDPLElWTSP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 95 PFE-AFKDseGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGG---HKGMELFVKRpefqaLRAG 170
Cdd:cd05680 87 PFEpVVRD--GRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEIGSpslPAFLEENAER-----LAAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 171 FAL--DEGLANPtDAFTVFYSER--SPWWIRVTSTGKPGHASRF--IEDTAAEKLHKVVNS---------ILAFREK--- 232
Cdd:cd05680 160 VVLvsDTSMWSP-DTPTITYGLRglAYLEISVTGPNRDLHSGSYggAVPNPANALARLLASlhdedgrvaIPGFYDDvrp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 233 ----ERQRLQANPHLKEGAVTSVNLTKLEGGVAYN---------------------------VVPATMSACFDFRVAPDV 281
Cdd:cd05680 239 ltdaEREAWAALPFDEAAFKASLGVPALGGEAGYTtlerlwarptldvngiwggyqgegsktVIPSKAHAKISMRLVPGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 282 DMKAFEKQLQSWCQE-AGEGVTFEFAQKF-TEPRMTPTDdtDPWWAAFSGACKEMNltlepeifpaATDSRYIRAVG-IP 358
Cdd:cd05680 319 DPDAIADLLEAHLRAhAPPGVTLSVKPLHgGRPYLVPTD--HPALQAAERALEEAF----------GKPPVFVREGGsIP 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 81884653 359 ALG-FSPMNRTPVLL----------HDHNERLHEAVFLRGVDIYTRLVAAL 398
Cdd:cd05680 387 IVAlFEKVLGIPTVLmgfglpddaiHAPNEKFRLECFHKGIEAIAHLLARL 437
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
37-399 |
1.54e-12 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 68.15 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 37 FLEERARQLGLSCQKIEVapGYVItvLTWPGTNPLLH-SILLNSHTDVVPVFKehwhHDPFEAFKDsEGYIYAR-----G 110
Cdd:COG2195 28 YLVEELKELGLEVEEDEA--GNVI--ATLPATPGYNVpTIGLQAHMDTVPQFP----GDGIKPQID-GGLITADgtttlG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 111 AQDmKS--VSIqyLEAVRRLKSEG--HRfprTIHMTFVPDEEVGGHkGMELF-VKRpeFQAlRAGFALDEGlanPTDAFT 185
Cdd:COG2195 99 ADD-KAgvAAI--LAALEYLKEPEipHG---PIEVLFTPDEEIGLR-GAKALdVSK--LGA-DFAYTLDGG---EEGELE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 186 V--FYSERspwwIRVTSTGKPGHASrfiedTAAEKLhkvVNSI-LAFrekerqRLQAnpHLKEGAV---TSVNLTKLEGG 259
Cdd:COG2195 166 YecAGAAD----AKITIKGKGGHSG-----DAKEKM---INAIkLAA------RFLA--ALPLGRIpeeTEGNEGFIHGG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 260 VAYNVVPATMSACFdfrVAPDVDMKAFEKQLQSW-------CQEAGEG-VTFEFAQKFtePRMTPTDDtDPWWAAFSGAC 331
Cdd:COG2195 226 SATNAIPREAEAVY---IIRDHDREKLEARKAELeeafeeeNAKYGVGvVEVEIEDQY--PNWKPEPD-SPIVDLAKEAY 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81884653 332 KEMNltLEPEIFP--AATDSRYIRAVGIPALGFSP--MNrtpvlLHDHNERLHEAVFLRGVDIYTRLVAALA 399
Cdd:COG2195 300 EELG--IEPKIKPirGGLDGGILSFKGLPTPNLGPggHN-----FHSPDERVSIESMEKAWELLVEILKLIA 364
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
15-379 |
2.76e-12 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 67.48 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 15 LFRQYLRICTvqPNPDYGSAVTFLEERARQLGLSCqKIEvAPGYVITVLTWPGTNpllhsILLNSHTDVVPVFKEhwhhd 94
Cdd:PRK08652 7 LLKQLVKIPS--PSGQEDEIALHIMEFLESLGYDV-HIE-SDGEVINIVVNSKAE-----LFVEVHYDTVPVRAE----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 95 PFEafkdSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIhmTFVPDEEVGGhKGMELFVKRpefqaLRAGFALd 174
Cdd:PRK08652 73 FFV----DGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGI--AFVSDEEEGG-RGSALFAER-----YRPKMAI- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 175 egLANPTDaFTVFYSERSPWWIRVTSTGKPGHASrFIEdtaaeklhKVVNSIL-AFREKERQRlQANPHLKEGAVTSVNL 253
Cdd:PRK08652 140 --VLEPTD-LKVAIAHYGNLEAYVEVKGKPSHGA-CPE--------SGVNAIEkAFEMLEKLK-ELLKALGKYFDPHIGI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 254 TKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWCQEAgeGVTFEFAQKFTEPRMTPTDDTDpwwAAFSGACKE 333
Cdd:PRK08652 207 QEIIGGSPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPILDEY--TVKYEYTEIWDGFELDEDEEIV---QLLEKAMKE 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 81884653 334 MNLTLEPEIFPAATDSRYIRAVGIPALGFSPMNRTpvLLHDHNERL 379
Cdd:PRK08652 282 VGLEPEFTVMRSWTDAINFRYNGTKTVVWGPGELD--LCHTKFERI 325
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
80-256 |
9.32e-12 |
|
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, Peptidase V (Xaa-His dipeptidase; PepV g.p. (Lactobacillus lactis); X-His dipeptidase; beta-Ala-His dipeptidase; carnosinase) subfamily. The PepV group of proteins is widely distributed in lactic acid bacteria. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminus, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity. The mammalian PepV also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Also included is the Staphylococcus aureus metallopeptidase, Sapep, a Mn(2+)-dependent dipeptidase where large interdomain movements could potentially regulate the activity of this enzyme.
Pssm-ID: 349884 [Multi-domain] Cd Length: 449 Bit Score: 66.50 E-value: 9.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 80 HTDVVPVfKEHWHHDPFEAFKDsEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGhKGMELFV 159
Cdd:cd03888 79 HLDVVPA-GEGWTTDPFKPVIK-DGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIFGTDEETGW-KCIEHYF 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 160 KR---PEFqalraGFALDeglANptdaFTVFYSERSPWWIRVTSTGKPGHASRFIEDTAAEKLHKV---VNSILAFREKE 233
Cdd:cd03888 156 EHeeyPDF-----GFTPD---AE----FPVINGEKGIVTVDLTFKIDDDKGYRLISIKGGEATNMVpdkAEAVIPGKDKE 223
|
170 180
....*....|....*....|...
gi 81884653 234 RQRLQANPHLKEGAVTSVNLTKL 256
Cdd:cd03888 224 ELALSAATDLKGNIEIDDGGVEL 246
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
13-398 |
1.06e-11 |
|
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE)/acetyl-lysine deacetylase (LysK) subfamily. Proteins in this subfamily are mainly archaeal with related bacterial species and are deacetylases with specificity for both N-acetyl-ornithine and N-acetyl-lysine found within a lysine biosynthesis operon. ArgE catalyzes the conversion of N-acetylornithine to ornithine, while LysK, a homolog of ArgE, has deacetylating activities for both N-acetyllysine and N-acetylornithine at almost equal efficiency. These results suggest that LysK which may share an ancestor with ArgE functions not only for lysine biosynthesis, but also for arginine biosynthesis in species such as Thermus thermophilus. The substrate specificity of ArgE is quite broad in that several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349904 [Multi-domain] Cd Length: 343 Bit Score: 65.45 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 13 VTLFRQYLRICTvqPNPDYGSAVTFLEERARQLGLSCQKIEVapGYVITVLtwpGTNPLLhsILLNSHTDVVPVFKEhwh 92
Cdd:cd05653 4 VELLLDLLSIYS--PSGEEARAAKFLEEIMKELGLEAWVDEA--GNAVGGA---GSGPPD--VLLLGHIDTVPGEIP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 93 hdpfeaFKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHrfpRTIHMTFVPDEEVGGHKGMELFVKRPEFQALRAGfa 172
Cdd:cd05653 72 ------VRVEGGVLYGRGAVDAKGPLAAMILAASALNEELG---ARVVVAGLVDEEGSSKGARELVRRGPRPDYIIIG-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 173 ldeglaNPTDAFTVFYSERSPWWIRVTSTGKPGHASRfIEDTAAEKLhkvvnsILAFREKERQRLQANPHLKEgaVTSVN 252
Cdd:cd05653 141 ------EPSGWDGITLGYRGSLLVKIRCEGRSGHSSS-PERNAAEDL------IKKWLEVKKWAEGYNVGGRD--FDSVV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 253 LTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWCQEAGEGVTfefaqKFTEPRMTPTDdtDPWWAAFSGACK 332
Cdd:cd05653 206 PTLIKGGESSNGLPQRAEATIDLRLPPRLSPEEAIALATALLPTCELEFI-----DDTEPVKVSKN--NPLARAFRRAIR 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81884653 333 EMNltLEPEIFPAATDSR---YIRAVGIPALGFSPMNrtPVLLHDHNERLHEAVFLRGVDIYTRLVAAL 398
Cdd:cd05653 279 KQG--GKPRLKRKTGTSDmnvLAPLWTVPIVAYGPGD--STLDHTPNEHIELAEIERAAAVLKGALEEL 343
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
188-302 |
1.07e-11 |
|
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices which make up the dimerization surface of members of the M20 family of peptidases. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 400158 [Multi-domain] Cd Length: 107 Bit Score: 61.21 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 188 YSERSPWWIRVTSTGKPGHASRFiedtaaeklHKVVNSILAFREKeRQRLQANPHLKEGAV--TSVNLTKLEGGVAYNVV 265
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAP---------GKGVNAIKLLARL-LAELPAEYGDIGFDFprTTLNITGIEGGTATNVI 70
|
90 100 110
....*....|....*....|....*....|....*..
gi 81884653 266 PATMSACFDFRVAPDVDMKAFEKQLQSWCQEAGEGVT 302
Cdd:pfam07687 71 PAEAEAKFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
35-208 |
4.65e-11 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 63.81 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 35 VTFLEERARQLGlsCQKIEVAP-----GYVitvltwpGTNPllHSILLNSHTDVVPVF-KEHWHHDPFEAFKDsEGYIYA 108
Cdd:PRK13004 38 VKRIKEEMEKVG--FDKVEIDPmgnvlGYI-------GHGK--KLIAFDAHIDTVGIGdIKNWDFDPFEGEED-DGRIYG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 109 RGAQDMKS--VSIQYleAVRRLKSEGHRFPRTIHMT-FVPDEEVGGHKGMELFVK---RPEFQAlragfaldegLANPTD 182
Cdd:PRK13004 106 RGTSDQKGgmASMVY--AAKIIKDLGLDDEYTLYVTgTVQEEDCDGLCWRYIIEEdkiKPDFVV----------ITEPTD 173
|
170 180
....*....|....*....|....*.
gi 81884653 183 aFTVFYSERSPWWIRVTSTGKPGHAS 208
Cdd:PRK13004 174 -LNIYRGQRGRMEIRVETKGVSCHGS 198
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
80-308 |
7.68e-11 |
|
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely related to the characterized non-specific dipeptidase, PepV. Many enzymes in this clade have been given names including the terms "Xaa-His" and "carnosinase" due to the early mis-characterization of the Lactobacillus delbrueckii PepV enzyme. These names are likely too specific.
Pssm-ID: 273854 [Multi-domain] Cd Length: 447 Bit Score: 63.55 E-value: 7.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 80 HTDVVPVfKEHWHHDPFEAFKDsEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGhKGMELFV 159
Cdd:TIGR01887 75 HLDVVPA-GDGWTSPPFEPTIK-DGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDEESGW-KCIDYYF 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 160 KRPEFQALraGFAldeglanPTDAFTVFYSERSpwwirvtstgkpghasrfiedtaaeklhkvvNSILAFrekerqrlqa 239
Cdd:TIGR01887 152 EHEEMPDI--GFT-------PDAEFPIIYGEKG-------------------------------ITTLEI---------- 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81884653 240 npHLKEGAVTSVNLTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAF----EKQLQSWCQEAGEGVTFEFAQK 308
Cdd:TIGR01887 182 --KFKDDTEGDVVLESFKAGEAYNMVPDHATAVISGKKLTEVEQLKFvffiAKELEGDFEVNDGTLTITLEGK 252
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
13-364 |
7.91e-11 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349900 [Multi-domain] Cd Length: 381 Bit Score: 63.21 E-value: 7.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 13 VTLFRQYLRICTvqPNPDYGSAVTFLEERARQLGLScqKIEVAP-GyviTVLTWPGTNPLLhsILLNSHTDVVPVF-KEH 90
Cdd:cd05649 1 TRFLRDLIQIPS--ESGEEKGVVERIEEEMEKLGFD--EVEIDPmG---NVIGYIGGGKKK--ILFDGHIDTVGIGnIDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 91 WHHDPFEAfKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHR-FPRTIHMTFVPDEEV-GGHKGMELFVK---RPEFQ 165
Cdd:cd05649 72 WKFDPYEG-YETDGKIYGRGTSDQKGGLASMVYAAKIMKDLGLRdFAYTILVAGTVQEEDcDGVCWQYISKAdkiKPDFV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 166 AlragfaldegLANPTDAfTVFYSERSPWWIRVTSTGKPGHASrfiedtAAEK----LHKVVNSILAFREKErQRLQANP 241
Cdd:cd05649 151 V----------SGEPTDG-NIYRGQRGRMEIRVDTKGVSCHGS------APERgdnaVYKMADIIQDIRQLN-PNFPEAP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 242 HLKEGAVTSVNLTKLEGGVayNVVPATMSACFDFRVAPDVDMKAFEKQLQSW--CQEAGEGVTFEFAQkFTEPRMT---- 315
Cdd:cd05649 213 FLGRGTLTVTDIFSTSPSR--CAVPDSCRISIDRRLTVGETWEGCLEEIRALpaVKKYGDDVAVSMYN-YDRPSYTgevy 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81884653 316 PTDDTDPWWA---------AFSGACKEMNLTlEPEI--FPAATDSRYI--RAvGIPALGFSP 364
Cdd:cd05649 290 ESERYFPTWLlpedhelvkALLEAYKALFGA-RPLIdkWTFSTNGVSImgRA-GIPCIGFGP 349
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
12-315 |
1.16e-10 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal and bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349935 [Multi-domain] Cd Length: 379 Bit Score: 62.49 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 12 SVTLFRQYLRICTVqpNPDYGSA--------VTFLEERARQLGLSCQKIEVAPGY--VITVLTWPGTNpllHSILLNSHT 81
Cdd:cd08013 3 PVSLTQTLVRINSS--NPSLSATggageaeiATYVAAWLAHRGIEAHRIEGTPGRpsVVGVVRGTGGG---KSLMLNGHI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 82 DVVPVfkEHWHHDPFEAfKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRfpRTIHMTFVPDEEVGGhKGMElfvkr 161
Cdd:cd08013 78 DTVTL--DGYDGDPLSG-EIADGRVYGRGTLDMKGGLAACMAALADAKEAGLR--GDVILAAVADEEDAS-LGTQ----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 162 pefQALRAGFALDEGL-ANPTDaFTVFYSERSPWWIRVTSTGKPGHASRfiEDTAAEKLHKVVNSILAFREKERQRLQAN 240
Cdd:cd08013 147 ---EVLAAGWRADAAIvTEPTN-LQIIHAHKGFVWFEVDIHGRAAHGSR--PDLGVDAILKAGYFLVALEEYQQELPERP 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81884653 241 PHLKEGAvTSVNLTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWCQE-AGEGVTFefaqKFTEPRMT 315
Cdd:cd08013 221 VDPLLGR-ASVHASLIKGGEEPSSYPARCTLTIERRTIPGETDESVLAELTAILGElAQTVPNF----SYREPRIT 291
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
80-212 |
4.54e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 61.25 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 80 HTDVVPVFKEH-WHHDPFEA-FKDseGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVgGHKGMEL 157
Cdd:PRK07205 83 HLDVVPEGDLSdWQTPPFEAvEKD--GCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIFGTDEET-LWRCMNR 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 81884653 158 FVKRPEFQALraGFAldeglanPTDAFTVFYSERSpwWIRVTSTGkPGHASRFIE 212
Cdd:PRK07205 160 YNEVEEQATM--GFA-------PDSSFPLTYAEKG--LLQAKLVG-PGSDQLELE 202
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
37-161 |
2.39e-09 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus.
Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 58.89 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 37 FLEERARQLGLSCQKIEvAPGYVITVLTWPGTNPllHSILLNSHTDVVPVFK-EHWHHDPFEAfKDSEGYIYARGAQDMK 115
Cdd:cd05681 27 FLKEFLRRLGAEVEIFE-TDGNPIVYAEFNSGDA--KTLLFYNHYDVQPAEPlELWTSDPFEL-TIRNGKLYARGVADDK 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 81884653 116 SVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGhKGMELFVKR 161
Cdd:cd05681 103 GELMARLAALRALLQHLGELPVNIKFLVEGEEEVGS-PNLEKFVAE 147
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
46-293 |
2.76e-09 |
|
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16)-related subfamily. Proteins in this subfamily have not yet been characterized, but have been predicted to have deacetylase activity. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349934 [Multi-domain] Cd Length: 423 Bit Score: 58.62 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 46 GLSCQKIEVAPGYVITVLTWPGTNPLLHSILLNSHTDVVPVFKEHWHHDPFEAFKDSEGyIYARGAQDMKSVSIQYLEAV 125
Cdd:cd08012 52 PLVIDHVSYVKGRGNIIVEYPGTVDGKTVSFVGSHMDVVTANPETWEFDPFSLSIDGDK-LYGRGTTDCLGHVALVTELF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 126 RRLKSEGHRFPRTIHMTFVPDEEVGG--HKGMELFVKRPEFQALRAG--FALDEGLANPtdafTVFYSERSPWwiRVTST 201
Cdd:cd08012 131 RQLATEKPALKRTVVAVFIANEENSEipGVGVDALVKSGLLDNLKSGplYWVDSADSQP----CIGTGGMVTW--KLTAT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 202 GKPGHASRfiedtaaekLHKVVNSILAFRE--KERQR---LQANPHLKE---GAVTSVNLT----KLEGGvAYNVVPATM 269
Cdd:cd08012 205 GKLFHSGL---------PHKAINALELVMEalAEIQKrfyIDFPPHPKEevyGFATPSTMKptqwSYPGG-SINQIPGEC 274
|
250 260
....*....|....*....|....
gi 81884653 270 SACFDFRVAPDVDMKAFEKQLQSW 293
Cdd:cd08012 275 TICGDCRLTPFYDVKEVREKLEEY 298
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
98-398 |
1.48e-08 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 55.95 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 98 AFKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFvkrpEFQALRAGFAL---- 173
Cdd:PRK07473 97 PWRREGNKCYGPGILDMKGGNYLALEAIRQLARAGITTPLPITVLFTPDEEVGTPSTRDLI----EAEAARNKYVLvpep 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 174 ---DEGLANPTDAFTVFyserspwwiRVTSTGKPGHASRFIEDTAAeklhkvvnsilAFREKERQRLQANPHLKEGAVTS 250
Cdd:PRK07473 173 grpDNGVVTGRYAIARF---------NLEATGRPSHAGATLSEGRS-----------AIREMARQILAIDAMTTEDCTFS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 251 VNLtkLEGGVAYNVVPATMS--ACFDFRVAPDVDmKAFEKQLQswCQEAGEGVTFEFAQKFTEPRMTPTDDTDPWWAAFS 328
Cdd:PRK07473 233 VGI--VHGGQWVNCVATTCTgeALSMAKRQADLD-RGVARMLA--LSGTEDDVTFTVTRGVTRPVWEPDAGTMALYEKAR 307
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81884653 329 GACKEMNLTLEPEIFPAATDSRYIRAVGIPAL-GFSPMNRTPVLLHDHNERlhEAVFLRGvdiytRLVAAL 398
Cdd:PRK07473 308 AIAGQLGLSLPHGSAGGGSDGNFTGAMGIPTLdGLGVRGADYHTLNEHIEV--DSLAERG-----RLMAGL 371
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
75-157 |
1.72e-07 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 52.85 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 75 ILLNSHTDVVPVFKEHWHHDPFEaFKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRfpRTIHMTFVPDEEVGGHKG 154
Cdd:PRK08554 66 LLFMAHFDVVPVNPEEWNTEPFK-LTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLN--GKVIFAFTGDEEIGGAMA 142
|
...
gi 81884653 155 MEL 157
Cdd:PRK08554 143 MHI 145
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
15-322 |
1.99e-07 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 52.48 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 15 LFRQYLRICTvqPNPDYGSAVTFLEERARQLGLSCQkievapgyvitvlTWPGTNPLLHS---ILLNSHTDVVPVFKEhw 91
Cdd:PRK00466 15 LLLDLLSIYT--PSGNETNATKFFEKISNELNLKLE-------------ILPDSNSFILGegdILLASHVDTVPGYIE-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 92 hhdPFEafkdsEGY-IYARGAQDMKSVSIQYLEAVRRLKSEGHRfprtIHMTFVPDEEVGGHKGMELFVKRPEFQALRAG 170
Cdd:PRK00466 78 ---PKI-----EGEvIYGRGAVDAKGPLISMIIAAWLLNEKGIK----VMVSGLADEESTSIGAKELVSKGFNFKHIIVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 171 faldeglaNPTDAFTVFYSERSPWWIRVTSTGKPGHASRfIEDTAAEKLHKVVNSILafrekERQRLQANPhlkegavtS 250
Cdd:PRK00466 146 --------EPSNGTDIVVEYRGSIQLDIMCEGTPEHSSS-AKSNLIVDISKKIIEVY-----KQPENYDKP--------S 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81884653 251 VNLTKLEGGVAYNVVPATMSACFDFRVApdvdMKAFEKQLQSwcqeagegvtfEFAQKFTEPRMTPTDDTDP 322
Cdd:PRK00466 204 IVPTIIRAGESYNVTPAKLYLHFDVRYA----INNKRDDLIS-----------EIKDKFQECGLKIVDETPP 260
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
13-161 |
2.16e-07 |
|
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase M20 family, CNDP (cytosolic nonspecific dipeptidase) subfamily including anserinase (Xaa-methyl-His dipeptidase, EC 3.4.13.5), 'serum' carnosinase (beta-alanyl-L-histidine dipeptidase; EC 3.4.13.20), and some uncharacterized proteins. Two genes, CN1 and CN2, coding for proteins that degrade carnosine (beta-alanyl-L-histidine) and homocarnosine (gamma-aminobutyric acid-L-histidine), two naturally occurring dipeptides with potential neuroprotective and neurotransmitter functions, have been identified. CN1 encodes for serum carnosinase and has narrow substrate specificity for Xaa-His dipeptides, where Xaa can be beta-alanine (carnosine), N-methyl beta-alanine, alanine, glycine and gamma-aminobutyric acid (homocarnosine). CN2 corresponds to the cytosolic nonspecific dipeptidase (CNDP; EC 3.4.13.18) and is not limited to Xaa-His dipeptides. CNDP requires Mn(2+) for full activity and does not hydrolyze homocarnosine. Anserinase is a dipeptidase that mainly catalyzes the hydrolysis of N-alpha-acetylhistidine.
Pssm-ID: 349925 [Multi-domain] Cd Length: 467 Bit Score: 52.60 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 13 VTLFRQYLRICTVQPNPDY----GSAVTFLEERARQLGLSCQKIEVAP-----GYVI----TVLTWPGTNPLLHSILLNS 79
Cdd:cd05676 13 IERLREAVAIQSVSADPEKrpelIRMMEWAAERLEKLGFKVELVDIGTqtlpdGEELplppVLLGRLGSDPSKKTVLIYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 80 HTDVVPVFKE-HWHHDPFEaFKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGhKGMELF 158
Cdd:cd05676 93 HLDVQPAKLEdGWDTDPFE-LTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCFEGMEESGS-EGLDEL 170
|
...
gi 81884653 159 VKR 161
Cdd:cd05676 171 IEA 173
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
15-186 |
3.66e-07 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 51.83 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 15 LFrQYLRICTVQPNPDYGS----AVTFLEERARQLGLSCQKIEvAPGYVITVLTWPGTNPLLHSILLNSHTDVVPVFK-E 89
Cdd:PRK09104 23 LF-ALLRIPSISTDPAYAAdcrkAADWLVADLASLGFEASVRD-TPGHPMVVAHHEGPTGDAPHVLFYGHYDVQPVDPlD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 90 HWHHDPFE-AFKDSEG---YIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGhKGMELFVKRpEFQ 165
Cdd:PRK09104 101 LWESPPFEpRIKETPDgrkVIVARGASDDKGQLMTFVEACRAWKAVTGSLPVRVTILFEGEEESGS-PSLVPFLEA-NAE 178
|
170 180
....*....|....*....|....
gi 81884653 166 ALRAGFAL--DEGLANP-TDAFTV 186
Cdd:PRK09104 179 ELKADVALvcDTGMWDReTPAITT 202
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
74-176 |
5.22e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 51.29 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 74 SILLNSHTDVVPVFK-EHWHHDPFEA-FKDseGYIYARGAQDMKSVSIQYLEAVRRLKSEgHRFPRTIHMTFVPDEEVGG 151
Cdd:PRK06446 64 TLLIYNHYDVQPVDPlSEWKRDPFSAtIEN--GRIYARGASDNKGTLMARLFAIKHLIDK-HKLNVNVKFLYEGEEEIGS 140
|
90 100
....*....|....*....|....*
gi 81884653 152 hKGMELFVKRPEfQALRAGFALDEG 176
Cdd:PRK06446 141 -PNLEDFIEKNK-NKLKADSVIMEG 163
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
75-291 |
5.49e-07 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 51.36 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 75 ILLNSHTDVVPvFKEH-WHHDPF---EAfkdsEGYIYARGAQDMKSVSIQYLEAVRRLksEGHRFPRTIHMTFVPDEEVG 150
Cdd:PRK05111 74 LLLAGHTDTVP-FDEGrWTRDPFtltEH----DGKLYGLGTADMKGFFAFILEALRDI--DLTKLKKPLYILATADEETS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 151 GHkGMELFVkrpEFQALRAGFALdegLANPTDAFTVF-----YSERspwwIRVtsTGKPGHASrfieD-----TAAEKLH 220
Cdd:PRK05111 147 MA-GARAFA---EATAIRPDCAI---IGEPTSLKPVRahkghMSEA----IRI--TGQSGHSS----DpalgvNAIELMH 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81884653 221 KVVNSILAFREKERQRLQaNPHLKEGAVTsVNLTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLQ 291
Cdd:PRK05111 210 DVIGELLQLRDELQERYH-NPAFTVPYPT-LNLGHIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLR 278
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
32-399 |
5.72e-07 |
|
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly(aspartic acid) hydrolase (PAA hydrolase)-like subfamily. PAA hydrolase enzymes are involved in alpha,beta-poly(D,L-aspartic acid) (tPAA) biodegradation. PAA is being extensively studied as a replacement for commercial polycarboxylate components since it can be degraded by enzymes from isolated tPAA degrading bacteria. Thus far, two types of PAA degrading bacteria (Sphingomonas sp. KT-1 and Pedobacter sp. KP-2) have been investigated in detail; the former can completely degrade tPAA of low-molecular weights below 5000, while the latter can degrade high molecular weight tPAA to release oligo(aspartic acid) (OAA) as a product, suggesting two kinds of PAA degrading enzymes. It has been shown that PAA hydrolase-1 from Sphingomonas sp. KT-1 hydrolyzes beta,beta-aspartic acid units in tPAA to produce OAA, and it is suggested that PAA hydrolase-2 hydrolyzes OAA to aspartic acid. Also included in this family is Bradyrhizobium 5-nitroanthranilic acid (5NAA)-aminohydrolase (5NAA-A), a biodegradation enzyme that converts 5NAA to 5-nitrosalicylic acid; 5NAA is a metabolite secreted by Streptomyces scabies, the bacterium responsible for potato scab, and metabolized by Bradyrhizobium species strain JS329.
Pssm-ID: 349891 [Multi-domain] Cd Length: 357 Bit Score: 50.94 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 32 GSAVTFLEERARQLGLSCQKIeVAPGYVITVLTWPGTNPllhSILLNSHTDVVpvFKEHwhhDPFEAFKDsEGYIYARGA 111
Cdd:cd03896 18 GARADLVAEWMADLGLGDVER-DGRGNVVGRLRGTGGGP---ALLFSAHLDTV--FPGD---TPATVRHE-GGRIYGPGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 112 QDMKSVSIQYLEAVRRLKSEGHRFPRTIHMT-FVPDEEVGGHKGMELFVKRpefQALRAGFALdegLANPTDaFTVFYSE 190
Cdd:cd03896 88 GDNKGSLACLLAMARAMKEAGAALKGDVVFAaNVGEEGLGDLRGARYLLSA---HGARLDYFV---VAEGTD-GVPHTGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 191 RSPWWIRVTSTGKPGHasRFIEDTAAEKLHKVVNSILAFREkerqrLQANphlkegAVTSVNLTKLEGGVAYNV--VPAT 268
Cdd:cd03896 161 VGSKRFRITTVGPGGH--SYGAFGSPSAIVAMAKLVEALYE-----WAAP------YVPKTTFAAIRGGGGTSVnrIANL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 269 MSACFDFRVAPDVDMKAFEKQLQSWCQEAGEGVTFEFAQ--KFTEPRMTPTDDTDPWWAAFSGACKEMNLTLEPEifPAA 346
Cdd:cd03896 228 CSMYLDIRSNPDAELADVQREVEAVVSKLAAKHLRVKARvkPVGDRPGGEAQGTEPLVNAAVAAHREVGGDPRPG--SSS 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 81884653 347 TDSRYIRAVGIPALGFSPMNRTPVllHDHNERLHEAVFLRGVDIYTRLVAALA 399
Cdd:cd03896 306 TDANPANSLGIPAVTYGLGRGGNA--HRGDEYVLKDDMLKGAKAYLMLAAALC 356
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
75-292 |
6.36e-07 |
|
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a large variety of enzymes, including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase), canosinase, DUG2 type proteins, as well as many proteins inferred by homology to be dipeptidases. These enzymes have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. Substrates of CNDP are varied and not limited to Xaa-His dipeptides. DUG2 proteins contain a metallopeptidase domain and a large N-terminal WD40 repeat region, and are involved in the alternative pathway of glutathione degradation.
Pssm-ID: 349888 [Multi-domain] Cd Length: 426 Bit Score: 51.17 E-value: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 75 ILLNSHTDVVPVFKEH-WHHDPFEAfKDSEGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMtFVPDEEVGGHK 153
Cdd:cd03893 66 VLLYGHYDVQPAGDEDgWDSDPFEL-TERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKF-IIEGEEESGSP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 154 GMELFV-KRPEFQALRAGFALDeGLANPTDAFTVFYSER--SPWWIRVTSTGKPGHASRF--IEDTAAEKLHKVVNSILA 228
Cdd:cd03893 144 SLDQLVeAHRDLLAADAIVISD-STWVGQEQPTLTYGLRgnANFDVEVKGLDHDLHSGLYggVVPDPMTALAQLLASLRD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 229 FR----------------EKERQRLQ------ANPHLKEGAVT-------SVNLTKLEGGV----AYNVVPATMSACFDF 275
Cdd:cd03893 223 ETgrilvpglydavrelpEEEFRLDAgvleevEIIGGTTGSVAerlwtrpALTVLGIDGGFpgegSKTVIPPRARAKISI 302
|
250
....*....|....*..
gi 81884653 276 RVAPDVDMKAFEKQLQS 292
Cdd:cd03893 303 RLVPGQDPEEASRLLEA 319
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
80-174 |
7.22e-07 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 50.99 E-value: 7.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 80 HTDVVPVfKEHWHHDPFEA-FKDseGYIYARGAQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEvGGHKGMELF 158
Cdd:PRK07318 87 HLDVVPA-GDGWDTDPYEPvIKD--GKIYARGTSDDKGPTMAAYYALKIIKELGLPLSKKVRFIVGTDEE-SGWKCMDYY 162
|
90
....*....|....*....
gi 81884653 159 VKR---PEFqalraGFALD 174
Cdd:PRK07318 163 FEHeeaPDF-----GFSPD 176
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
75-312 |
3.05e-06 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 48.81 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 75 ILLNSHTDVVpvF-KEHwhhdPFEAFKD-SEGYIYARGAQDMKSVSIQYLEAVRRLksEGHRFPRTIHMTFV--PDEEVG 150
Cdd:PRK07338 95 VLLTGHMDTV--FpADH----PFQTLSWlDDGTLNGPGVADMKGGIVVMLAALLAF--ERSPLADKLGYDVLinPDEEIG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 151 GhkgmelFVKRPEFQALRAGF--------ALDEG-LANPTDAFTVFyserspwwiRVTSTGKPGHASRFIEDTAaeklhk 221
Cdd:PRK07338 167 S------PASAPLLAELARGKhaaltyepALPDGtLAGARKGSGNF---------TIVVTGRAAHAGRAFDEGR------ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 222 vvNSILAFREKErQRLQANPHLKEGavTSVNLTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWCQE--AGE 299
Cdd:PRK07338 226 --NAIVAAAELA-LALHALNGQRDG--VTVNVAKIDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQvnQRH 300
|
250
....*....|...
gi 81884653 300 GVTFEFAQKFTEP 312
Cdd:PRK07338 301 GVSLHLHGGFGRP 313
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
67-155 |
9.64e-06 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 47.72 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 67 GTNPLLHSILLNSHTDVVPV-------------------FKEHWHHDPFEAFKD--SEGYIYARGAQDMKSVSIQYLEAV 125
Cdd:cd05654 66 GKKPSKRTIILISHFDTVGIedygelkdiafdpdeltkaFSEYVEELDEEVREDllSGEWLFGRGTMDMKSGLAVHLALL 145
|
90 100 110
....*....|....*....|....*....|
gi 81884653 126 RRLkSEGHRFPRTIHMTFVPDEEVgGHKGM 155
Cdd:cd05654 146 EQA-SEDEDFDGNLLLMAVPDEEV-NSRGM 173
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
34-164 |
8.18e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 44.51 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 34 AVTFLEERARQLGLSCQKIEVAPGYVITVLTWPGtNPLLHSILLNSHTDVVPVFKE-HWHHDPFEAfKDSEGYIYARGAQ 112
Cdd:PRK07907 46 SAEWVADLLREAGFDDVRVVSADGAPAVIGTRPA-PPGAPTVLLYAHHDVQPPGDPdAWDSPPFEL-TERDGRLYGRGAA 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 81884653 113 DMKSVSIQYLEAVRRLkseGHRFPRTIHMtFVPDEEVGGHKGMELFVK-RPEF 164
Cdd:PRK07907 124 DDKGGIAMHLAALRAL---GGDLPVGVTV-FVEGEEEMGSPSLERLLAeHPDL 172
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
122-395 |
1.40e-04 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 43.74 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 122 LEAVRRLKSEGHRFPRTIHMTFVPDEEV-GGHKGM--ELFVKRPEFQALrAGFALDEGLANPTDAFT---VFYSERSpww 195
Cdd:cd03886 98 LGAAKLLAERRDPLKGTVRFIFQPAEEGpGGAKAMieEGVLENPGVDAA-FGLHVWPGLPVGTVGVRsgaLMASADE--- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 196 IRVTSTGKPGHASRfiedtaaekLHKVVNSILAFREKErQRLQA-----NPHLKEGAVTsvnLTKLEGGVAYNVVP--AT 268
Cdd:cd03886 174 FEITVKGKGGHGAS---------PHLGVDPIVAAAQIV-LALQTvvsreLDPLEPAVVT---VGKFHAGTAFNVIPdtAV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 269 MSAcfDFRVAPDVDMKAFEKQLQSWCQEAGE--GVTFEFAQKFTEPrmtPTDDTDPWWAAFSGACKEM---NLTLEPEIF 343
Cdd:cd03886 241 LEG--TIRTFDPEVREALEARIKRLAEGIAAayGATVELEYGYGYP---AVINDPELTELVREAAKELlgeEAVVEPEPV 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 81884653 344 PAATDSRYIrAVGIPA----LGFSPMNRTPVLLHDHNERLHEAVFLRGVDIYTRLV 395
Cdd:cd03886 316 MGSEDFAYY-LEKVPGaffwLGAGEPDGENPGLHSPTFDFDEDALPIGAALLAELA 370
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
17-150 |
1.45e-04 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 43.97 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 17 RQYLRICTV----QPNPDYGSAVTFLEERARQLGLSCQKIEVAPGYVITVLTWpgtnplLH-----SILLNSHTDVVPVF 87
Cdd:PRK08201 21 KEFLRIPSIsalsEHKEDVRKAAEWLAGALEKAGLEHVEIMETAGHPIVYADW------LHapgkpTVLIYGHYDVQPVD 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81884653 88 KEH-WHHDPFEAfKDSEGYIYARGAQDMKSVSIQYLEAVRR-LKSEGhRFPRTIHMTFVPDEEVG 150
Cdd:PRK08201 95 PLNlWETPPFEP-TIRDGKLYARGASDDKGQVFMHLKAVEAlLKVEG-TLPVNVKFCIEGEEEIG 157
|
|
| M20_Acy1-like |
cd08660 |
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and ... |
201-394 |
1.66e-03 |
|
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and Aminoacylase 1-like protein 2 (ACY1L2). Aminoacylase 1 proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. ACY1 (acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1L2 family contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in E. coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D) resulting in a metabolic disorder manifesting with encephalopathy and psychomotor delay.
Pssm-ID: 349945 [Multi-domain] Cd Length: 366 Bit Score: 40.30 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 201 TGKPGHASrfIEDTAAEKLHKVVNSILAFRekerQRLQANPHLKEGAVTSVnlTKLEGGVAYNVVPATMSACFDFRVAPD 280
Cdd:cd08660 178 KGKGGHAS--IPNNSIDPIAAAGQIISGLQ----SVVSRNISSLQNAVVSI--TRVQGGTAWNVIPDQAE*EGTVRAFTK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 281 VDMKAFEKQLQSWC--QEAGEGVTFEFaqKFTEPRMTPTDDTDPWWAAFSGACKEM-NLTLEPEIFPAATDSRYIRAVgI 357
Cdd:cd08660 250 EARQAVPEH*RRVAegIAAGYGCQAEF--KWFPNGPSEVQNDGTLLNAFSKAAARLgYATVHAEQSPGSEDFALYQEK-I 326
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 81884653 358 PalGFSP---MNRTPVLLHDHNERLHEAVFLRGVDIYTRL 394
Cdd:cd08660 327 P--GFFVw*gTNGRTEEWHHPAFRLDEEALTVGAQIFAEL 364
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
122-305 |
2.55e-03 |
|
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of those sequences detected by pfam01546. Included within this group are hydrolases of hippurate (N-benzylglycine), indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. These hydrolases are of the carboxypeptidase-type, most likely utilizing a zinc ion in the active site. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273857 [Multi-domain] Cd Length: 363 Bit Score: 39.64 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 122 LEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHK----------------GMELFVKRPEFQ-ALRAGFaldegLANPTDAF 184
Cdd:TIGR01891 99 LGTAKLLKKLADLLEGTVRLIFQPAEEGGGGAtkmiedgvlddvdailGLHPDPSIPAGTvGLRPGT-----IMAAADKF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 185 TVFYserspwwirvtsTGKPGHASRfiedtaaekLHKVVNSIL-------AFREKERQRLQANphlkEGAVTSVnlTKLE 257
Cdd:TIGR01891 174 EVTI------------HGKGAHAAR---------PHLGRDALDaaaqlvvALQQIVSRNVDPS----RPAVVSV--GIIE 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 81884653 258 GGVAYNVVPATMSACFDFRVAPDVDMKAFEKQLQSWCQEAGE--GVTFEF 305
Cdd:TIGR01891 227 AGGAPNVIPDKASMSGTVRSLDPEVRDQIIDRIERIVEGAAAmyGAKVEL 276
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
38-161 |
2.83e-03 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 39.95 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 38 LEERARQLGLSCQKIevapGYVITVLTWPGTNPLLHSILlnSHTDVVPVFKEHW-----HHDPFEAFKDSEgYIYARGAQ 112
Cdd:PRK06156 81 LKSLARDFGLDYRNV----DNRVLEIGLGGSGSDKVGIL--THADVVPANPELWvldgtRLDPFKVTLVGD-RLYGRGTE 153
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 81884653 113 DMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGhKGMELFVKR 161
Cdd:PRK06156 154 DDKGAIVTALYAMKAIKDSGLPLARRIELLVYTTEETDG-DPLKYYLER 201
|
|
| PRK12890 |
PRK12890 |
allantoate amidohydrolase; Reviewed |
38-326 |
3.98e-03 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 237248 [Multi-domain] Cd Length: 414 Bit Score: 39.12 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 38 LEERARQLGLSCQkIEVApGYVItvLTWPGTNPLLHSILLNSHTDVVPvfkehwhhdpfeafkdsEGyiyarGAQDMKSV 117
Cdd:PRK12890 44 LAAWMRAAGLEVR-RDAA-GNLF--GRLPGRDPDLPPLMTGSHLDTVP-----------------NG-----GRYDGILG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 118 SIQYLEAVRRLKSEGHRFPRTIHMTFVPDEE--------VG-----GHKGME--LFVKRPEFQAL-----RAGFALD--E 175
Cdd:PRK12890 98 VLAGLEVVAALREAGIRPPHPLEVIAFTNEEgvrfgpsmIGsralaGTLDVEavLATRDDDGTTLaealrRIGGDPDalP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 176 GLANP---TDAFTVFYSERSP------------------WWIRVTSTGKPGHAS------------------RFIEDTAA 216
Cdd:PRK12890 178 GALRPpgaVAAFLELHIEQGPvleaeglpigvvtaiqgiRRQAVTVEGEANHAGttpmdlrrdalvaaaelvTAMERRAR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884653 217 EKLHKVVNSIlafrekerQRLQANPHlkegavtsvnltkleggvAYNVVPATMSACFDFRvAPDVD-MKAFEKQLQSWCQ 295
Cdd:PRK12890 258 ALLHDLVATV--------GRLDVEPN------------------AINVVPGRVVFTLDLR-SPDDAvLEAAEAALLAELE 310
|
330 340 350
....*....|....*....|....*....|...
gi 81884653 296 --EAGEGVTFEFAqKFTEPRMTPtddTDPWWAA 326
Cdd:PRK12890 311 aiAAARGVRIELE-RLSRSEPVP---CDPALVD 339
|
|
| |
